The stratified squamous epithelia of the ocular surface, larynx, and v
agina are mucus-coated epithelia, apices of which are subject to abras
ive pressure from epithelia - epithelia interactions from eyelid, voca
l cords, or vaginal folds, respectively. Mucus coats on these epitheli
a have generally been considered to be derived from the specialized mu
cin-producing cells embedded either in the epithelia or in adjacent ti
ssues. Here we report the isolation, partial characterization, and cel
lular localization of a mucin-like glycoprotein produced by these stra
tified epithelia. In all three epithelia, the mucin-like molecule is p
resent on cytoplasmic vesicles in subapical cells. As cells differenti
ate to their apical-most position adjacent to their mucus coat, the mu
cin-like molecule moves to the cell membrane where it is particularly
prominent on microplicae folds. Lectin affinity chromatography was use
d to isolate the molecule from rat vaginal and corneal epithelium. Iso
lated material was approximately 60% carbohydrate and 40% protein. The
major monosaccharide was N-acetylgalactosamine with lesser amounts of
N-acetylglucosamine, galactose, mannose, xylose and fucose. Amino aci
d analysis demonstrated the predominant amino acids to be glycine, ser
ine, threonine and proline. These data plus PAS and Alcian blue bindin
g to the isolate indicate a mucin-like glycoprotein.